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Entry version 183 (08 May 2019)
Sequence version 2 (18 Oct 2001)
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Protein

Protective antigen

Gene

pagA

Organism
Bacillus anthracis
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. PA binds to a receptor (ATR) in sensitive eukaryotic cells, thereby facilitating the translocation of the enzymatic toxin components, edema factor and lethal factor, across the target cell membrane. PA associated with LF causes death when injected, PA associated with EF produces edema. PA induces immunity to infection with anthrax.

Miscellaneous

In PubMed:10085028 multiple mutagenesis experiments were performed that showed that the residues present in the small loop of domain 4, and not the ones in the large loop, are involved in receptor recognition. In PubMed:14623961 high-throughput scanning mutagenesis experiments were performed in which all residues of PA-63 were mutated into Cys. Dominantly negative (DN) mutants were all clustered in domain 2. DN mutants prevent the conformational transition of PA-63 from the prepore to the pore state.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi206Calcium1
Metal bindingi208Calcium1
Metal bindingi210Calcium1
Metal bindingi217Calcium1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei712Essential for binding to cell receptor1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionToxin
Biological processVirulence
LigandCalcium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ANTHRA:GBAA_PXO1_0164-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5210891 Uptake and function of anthrax toxins

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.C.42.1.1 the channel-forming bacillus anthracis protective antigen (bapa) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protective antigen
Short name:
PA
Alternative name(s):
Anthrax toxins translocating protein
PA-83
Short name:
PA83
Cleaved into the following 2 chains:
Protective antigen PA-20
Short name:
PA20
Protective antigen PA-63
Short name:
PA63
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:pagA
Synonyms:pag
Ordered Locus Names:pXO1-110, BXA0164, GBAA_pXO1_0164
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pXO10 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus anthracis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1392 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000594 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Plasmid pXO1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

  • Secreted
  • Note: Secreted through the Sec-dependent secretion pathway. Therefore, PA is translocated across the membrane in an unfolded state and then it is folded into its native configuration on the trans side of the membrane, prior to its release to the environment. PA requires the extracellular chaperone PrsA for efficient folding.1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi213P → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 1 Publication1
Mutagenesisi216L → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 1 Publication1
Mutagenesisi231F → A: Loss of ability to bind to LF and completely non-toxic. 1 Publication1
Mutagenesisi232L → A: Loss of ability to bind to LF and completely non-toxic. 1 Publication1
Mutagenesisi234P → A: Loss of ability to bind to LF and completely non-toxic. 1 Publication1
Mutagenesisi236I → A: Loss of ability to bind to LF and completely non-toxic. 1 Publication1
Mutagenesisi239I → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 1 Publication1
Mutagenesisi255W → A: No effect on LF-binding ability and as toxic as the wild-type. 1 Publication1
Mutagenesisi265F → A: No effect on LF-binding ability and as toxic as the wild-type. 1 Publication1
Mutagenesisi289P → A: Reduced toxicity in combination with lethal factor. Decreased membrane insertion and translocation of LF. 1 Publication1
Mutagenesisi342 – 344FFD → AAA: Decrease in toxicity probably due to slow translocation of LF. 1 Publication3
Mutagenesisi342 – 343Missing : Loss of toxicity probably due to loss of capability to translocate LF. 1 Publication2
Mutagenesisi342F → C: Loss of toxicity probably due to loss of capability to translocate LF. 1 Publication1
Mutagenesisi344D → A: Decrease in toxicity probably due to slow translocation of LF. 1 Publication1
Mutagenesisi375W → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. 1 Publication1
Mutagenesisi379M → A: No effect. 1 Publication1
Mutagenesisi381L → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. 1 Publication1
Mutagenesisi393I → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi409T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi411S → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi422T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi426K → A or D: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications1
Mutagenesisi428N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi440Y → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi451N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi454D → A or K: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications1
Mutagenesisi456F → A: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications1
Mutagenesisi512Q → A: Loss of heptamerization capability. 1 Publication1
Mutagenesisi541D → A: Loss of heptamerization capability. 1 Publication1
Mutagenesisi543L → A: Decrease in heptamerization capability. 1 Publication1
Mutagenesisi581F → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi583F → A: Decrease in toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi591I → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi595L → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi603I → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi621R → A: No effect. 1 Publication1
Mutagenesisi686N → A: Decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi708K → A: No effect on toxicity. 1 Publication1
Mutagenesisi709K → A: Slight decrease in toxicity. 1 Publication1
Mutagenesisi710Y → A: Great decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi711N → A: Loss of toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi712D → A: Loss of toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi713K → A: No effect on toxicity. 1 Publication1
Mutagenesisi714L → A: No effect on toxicity. 1 Publication1
Mutagenesisi715P → A: Great decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi716L → A: Decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi717Y → A: No effect on toxicity. 1 Publication1
Mutagenesisi718I → A: Decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi719S → A: No effect on toxicity. 1 Publication1
Mutagenesisi720N → A: No effect on toxicity. 1 Publication1
Mutagenesisi721P → A: No effect on toxicity. 1 Publication1
Mutagenesisi722N → A: No effect on toxicity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5352

Drug and drug target database

More...
DrugBanki
DB09057 Anthrax immune globulin human
DB08902 Raxibacumab

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 29Add BLAST29
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002199630 – 764Protective antigenAdd BLAST735
ChainiPRO_000002199730 – 196Protective antigen PA-20Add BLAST167
ChainiPRO_0000021998197 – 764Protective antigen PA-63Add BLAST568

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytic activation by furin or a furin-like protease cleaves the protein in two parts, PA-20 and PA-63; the latter is the mature protein. The cleavage occurs at the cell surface and probably in the serum of infected animals as well; both native and cleaved PA are able to bind to the cell receptor. The release of PA20 from the remaining receptor-bound PA63 exposes the binding site for EF and LF, and promotes oligomerization and internalization of the protein.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei196 – 197Cleavage; by furin2
Sitei343 – 344Cleavage; by chymotrypsin; required for translocation of LF and EF2

Keywords - PTMi

Cleavage on pair of basic residues

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P13423

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P13423

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Anthrax toxins are composed of three distinct proteins, a protective antigen (PA), a lethal factor (LF) and an edema factor (EF). None of these is toxic by itself. PA+LF forms the lethal toxin (LeTx); PA+EF forms the edema toxin (EdTx). PA-63 forms heptamers and this oligomerization is required for LF or EF binding. This complex is endocytosed by the host. Once activated, at low pH, the heptamer undergoes conformational changes and converts from prepore to pore inserted in the membrane, forming cation-selective channels and triggering the release of LF and EF in the host cytoplasm.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-29841N

Protein interaction database and analysis system

More...
IntActi
P13423, 16 interactors

Molecular INTeraction database

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MINTi
P13423

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P13423

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1764
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ACCX-ray2.10A30-764[»]
1T6BX-ray2.50X30-764[»]
1TX5model-C30-764[»]
1TZNX-ray4.30A/B/C/D/E/F/G/H/I/J/K/L/M/O203-764[»]
1TZOX-ray3.60A/B/C/D/E/F/G/H/I/J/K/L/M/O203-764[»]
1V36model-A/B/C/D/E/F/G197-764[»]
3ETBX-ray3.80J/K/L/M621-764[»]
3INOX-ray1.95A/B624-764[»]
3J9Celectron microscopy2.90A203-764[»]
3KWVX-ray3.10A/B/D/E197-764[»]
3MHZX-ray1.70A30-764[»]
3Q8AX-ray3.13A30-764[»]
3Q8BX-ray2.00A30-764[»]
3Q8CX-ray2.85A30-764[»]
3Q8EX-ray2.10A30-764[»]
3Q8FX-ray2.10A30-764[»]
3TEWX-ray1.45A30-764[»]
3TEXX-ray1.70A30-764[»]
3TEYX-ray2.12A30-764[»]
3TEZX-ray1.83A30-764[»]
4EE2X-ray1.91A30-764[»]
4H2AX-ray1.62A30-764[»]
4NAMX-ray1.70A30-764[»]
5FR3X-ray1.94A43-764[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P13423

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P13423

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini43 – 179PA14PROSITE-ProRule annotationAdd BLAST137

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni30 – 287Domain 1, calcium-binding; LF and EF binding sitesAdd BLAST258
Regioni288 – 516Domain 2, membrane insertion and heptamerizationAdd BLAST229
Regioni517 – 624Domain 3, heptamerizationAdd BLAST108
Regioni625 – 764Domain 4, binding to the receptorAdd BLAST140

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The molecule is folded into four functional domains. Each domain is required for a particular step in the toxicity process. Domain 1 contains two calcium ions and the proteolytic activation site. Cleavage of the PA monomer releases the subdomain 1a, which is the N-terminal fragment of 20-kDa (PA20). The subdomain 1b is part of the remaining 63-kDa fragment (PA63) and contains the binding sites for LP and EF. Domain 2 is a beta-barrel core containing a large flexible loop that has been implicated in membrane insertion and pore formation. There is a chymotrypsin cleavage site in this loop that is required for toxicity. Domain 3 has a hydrophobic patch thought to be involved in protein-protein interactions. Domain 4 appears to be a separate domain and shows limited contact with the other three domains: it would swing out of the way during membrane insertion. It is required for binding to the receptor; the small loop is involved in receptor recognition.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the bacterial binary toxin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000034566

KEGG Orthology (KO)

More...
KOi
K11030

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.240, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003896 Bacterial_exotoxin_B
IPR035331 Binary_toxB_3
IPR037524 PA14/GLEYA
IPR011658 PA14_dom
IPR035088 PA_Ca-bd
IPR027439 PA_heptamer_dom
IPR037149 PA_heptamer_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03495 Binary_toxB, 1 hit
PF17475 Binary_toxB_2, 1 hit
PF17476 Binary_toxB_3, 1 hit
PF07691 PA14, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01391 BINARYTOXINB

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00758 PA14, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51820 PA14, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P13423-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKRKVLIPL MALSTILVSS TGNLEVIQAE VKQENRLLNE SESSSQGLLG
60 70 80 90 100
YYFSDLNFQA PMVVTSSTTG DLSIPSSELE NIPSENQYFQ SAIWSGFIKV
110 120 130 140 150
KKSDEYTFAT SADNHVTMWV DDQEVINKAS NSNKIRLEKG RLYQIKIQYQ
160 170 180 190 200
RENPTEKGLD FKLYWTDSQN KKEVISSDNL QLPELKQKSS NSRKKRSTSA
210 220 230 240 250
GPTVPDRDND GIPDSLEVEG YTVDVKNKRT FLSPWISNIH EKKGLTKYKS
260 270 280 290 300
SPEKWSTASD PYSDFEKVTG RIDKNVSPEA RHPLVAAYPI VHVDMENIIL
310 320 330 340 350
SKNEDQSTQN TDSQTRTISK NTSTSRTHTS EVHGNAEVHA SFFDIGGSVS
360 370 380 390 400
AGFSNSNSST VAIDHSLSLA GERTWAETMG LNTADTARLN ANIRYVNTGT
410 420 430 440 450
APIYNVLPTT SLVLGKNQTL ATIKAKENQL SQILAPNNYY PSKNLAPIAL
460 470 480 490 500
NAQDDFSSTP ITMNYNQFLE LEKTKQLRLD TDQVYGNIAT YNFENGRVRV
510 520 530 540 550
DTGSNWSEVL PQIQETTARI IFNGKDLNLV ERRIAAVNPS DPLETTKPDM
560 570 580 590 600
TLKEALKIAF GFNEPNGNLQ YQGKDITEFD FNFDQQTSQN IKNQLAELNA
610 620 630 640 650
TNIYTVLDKI KLNAKMNILI RDKRFHYDRN NIAVGADESV VKEAHREVIN
660 670 680 690 700
SSTEGLLLNI DKDIRKILSG YIVEIEDTEG LKEVINDRYD MLNISSLRQD
710 720 730 740 750
GKTFIDFKKY NDKLPLYISN PNYKVNVYAV TKENTIINPS ENGDTSTNGI
760
KKILIFSKKG YEIG
Length:764
Mass (Da):85,811
Last modified:October 18, 2001 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3AE1EFBF48FAA03F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti314Q → E in AAA22637 (PubMed:3148491).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti295M → I in strain: PAI. 1
Natural varianti392N → D in strain: PAI. 1
Natural varianti560F → L in Sverdlovsk sample. 1
Natural varianti565P → S in strain: BA1024. 1
Natural varianti600A → V in strain: BA1024, V770-NP1-R, Carbosap and Ferrara. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M22589 Genomic DNA Translation: AAA22637.1
AF306778 Genomic DNA Translation: AAG24446.1
AF306779 Genomic DNA Translation: AAG24447.1
AF306780 Genomic DNA Translation: AAG24448.1
AF306781 Genomic DNA Translation: AAG24449.1
AF306782 Genomic DNA Translation: AAG24450.1
AF306783 Genomic DNA Translation: AAG24451.1
AF268967 Genomic DNA Translation: AAF86457.1
AF065404 Genomic DNA Translation: AAD32414.1
AE011190 Genomic DNA Translation: AAM26109.1
AE017336 Genomic DNA Translation: AAT28905.2
AJ413936 Genomic DNA Translation: CAC93934.1
AJ413937 Genomic DNA Translation: CAC93935.1
AB125961 Genomic DNA Translation: BAD14937.1

Protein sequence database of the Protein Information Resource

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PIRi
I39934

NCBI Reference Sequences

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RefSeqi
NP_052806.1, NC_001496.1
WP_000746486.1, NZ_QPKQ01000017.1
WP_000746487.1, NZ_QAEM01000007.1
WP_000746488.1, NZ_QANP01000007.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAM26109; AAM26109; BX_A0164
AAT28905; AAT28905; GBAA_pXO1_0164

Database of genes from NCBI RefSeq genomes

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GeneIDi
3361714

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bar:GBAA_pXO1_0164

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22589 Genomic DNA Translation: AAA22637.1
AF306778 Genomic DNA Translation: AAG24446.1
AF306779 Genomic DNA Translation: AAG24447.1
AF306780 Genomic DNA Translation: AAG24448.1
AF306781 Genomic DNA Translation: AAG24449.1
AF306782 Genomic DNA Translation: AAG24450.1
AF306783 Genomic DNA Translation: AAG24451.1
AF268967 Genomic DNA Translation: AAF86457.1
AF065404 Genomic DNA Translation: AAD32414.1
AE011190 Genomic DNA Translation: AAM26109.1
AE017336 Genomic DNA Translation: AAT28905.2
AJ413936 Genomic DNA Translation: CAC93934.1
AJ413937 Genomic DNA Translation: CAC93935.1
AB125961 Genomic DNA Translation: BAD14937.1
PIRiI39934
RefSeqiNP_052806.1, NC_001496.1
WP_000746486.1, NZ_QPKQ01000017.1
WP_000746487.1, NZ_QAEM01000007.1
WP_000746488.1, NZ_QANP01000007.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ACCX-ray2.10A30-764[»]
1T6BX-ray2.50X30-764[»]
1TX5model-C30-764[»]
1TZNX-ray4.30A/B/C/D/E/F/G/H/I/J/K/L/M/O203-764[»]
1TZOX-ray3.60A/B/C/D/E/F/G/H/I/J/K/L/M/O203-764[»]
1V36model-A/B/C/D/E/F/G197-764[»]
3ETBX-ray3.80J/K/L/M621-764[»]
3INOX-ray1.95A/B624-764[»]
3J9Celectron microscopy2.90A203-764[»]
3KWVX-ray3.10A/B/D/E197-764[»]
3MHZX-ray1.70A30-764[»]
3Q8AX-ray3.13A30-764[»]
3Q8BX-ray2.00A30-764[»]
3Q8CX-ray2.85A30-764[»]
3Q8EX-ray2.10A30-764[»]
3Q8FX-ray2.10A30-764[»]
3TEWX-ray1.45A30-764[»]
3TEXX-ray1.70A30-764[»]
3TEYX-ray2.12A30-764[»]
3TEZX-ray1.83A30-764[»]
4EE2X-ray1.91A30-764[»]
4H2AX-ray1.62A30-764[»]
4NAMX-ray1.70A30-764[»]
5FR3X-ray1.94A43-764[»]
SMRiP13423
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29841N
IntActiP13423, 16 interactors
MINTiP13423

Chemistry databases

BindingDBiP13423
ChEMBLiCHEMBL5352
DrugBankiDB09057 Anthrax immune globulin human
DB08902 Raxibacumab

Protein family/group databases

TCDBi1.C.42.1.1 the channel-forming bacillus anthracis protective antigen (bapa) family

Proteomic databases

PRIDEiP13423

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM26109; AAM26109; BX_A0164
AAT28905; AAT28905; GBAA_pXO1_0164
GeneIDi3361714
KEGGibar:GBAA_pXO1_0164

Phylogenomic databases

HOGENOMiHOG000034566
KOiK11030

Enzyme and pathway databases

BioCyciANTHRA:GBAA_PXO1_0164-MONOMER
ReactomeiR-HSA-5210891 Uptake and function of anthrax toxins

Miscellaneous databases

EvolutionaryTraceiP13423
PMAP-CutDBiP13423

Protein Ontology

More...
PROi
PR:P13423

Family and domain databases

Gene3Di2.60.120.240, 1 hit
InterProiView protein in InterPro
IPR003896 Bacterial_exotoxin_B
IPR035331 Binary_toxB_3
IPR037524 PA14/GLEYA
IPR011658 PA14_dom
IPR035088 PA_Ca-bd
IPR027439 PA_heptamer_dom
IPR037149 PA_heptamer_dom_sf
PfamiView protein in Pfam
PF03495 Binary_toxB, 1 hit
PF17475 Binary_toxB_2, 1 hit
PF17476 Binary_toxB_3, 1 hit
PF07691 PA14, 1 hit
PRINTSiPR01391 BINARYTOXINB
SMARTiView protein in SMART
SM00758 PA14, 1 hit
PROSITEiView protein in PROSITE
PS51820 PA14, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPAG_BACAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P13423
Secondary accession number(s): Q937W2
, Q937W3, Q9F5R7, Q9KH69, Q9RQU2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 18, 2001
Last modified: May 8, 2019
This is version 183 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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